The mechanisms of conformation change in proteins and polynucleotides are to be studied experimentally and theoretically. The focus of this work is to be the characterization of the intermediate partially ordered states on the pathway between fully ordered, native and the disordered, denatured conformations. Several methods for studying the kinetics of conformational reactions using minimum peturbations of state are being developed for this purpose. One of these involves the measurement of chemical kinetics in systems resting unperturbed at chemical equilibrium by observations of the rates of decay of spontaneous concentration fluctuations. Theoretical models of the kinetics of sequential, multi-step processes are being explored and applied to the interpretation of recent experimental studies of the kinetics of folding of small globular proteins.